zantrin Z3 | 312742-16-8

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 二氮杂萘
• 英文名称: zantrin Z3
• 英文别名: N-[2-[2-(4-chlorophenyl)ethenyl]benzo[g]quinazolin-4-yl]-N',N'-diethylethane-1,2-diamine
• CAS: 312742-16-8
• 化学式: C₂₆H₂₇ClN₄
• mdl: MFCD00226996
• 分子量: 430.98
• InChiKey: MSOORHLGOVMZQM-UHFFFAOYSA-N

物化性质

• 沸点：
  548.1±50.0 °C(Predicted)
• 密度：
  1.236±0.06 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  6.5
• 重原子数：
  31
• 可旋转键数：
  8
• 环数：
  4.0
• sp3杂化的碳原子比例：
  0.23
• 拓扑面积：
  41
• 氢给体数：
  1
• 氢受体数：
  4

反应信息

• 作为产物：
  描述：

  2-methylbenzo[g]quinazolin-4(3H)-one 在 4-二甲氨基吡啶 、 溶剂黄146 、 N,N-二甲基苯胺 、 三乙胺 、 三氯氧磷 作用下， 以 甲苯 为溶剂， 反应 12.0h， 生成 zantrin Z3
  参考文献：
  名称：

  Comparison of Small Molecule Inhibitors of the Bacterial Cell Division Protein FtsZ and Identification of a Reliable Cross-Species Inhibitor

  摘要：

  ZFtsZ is a guanosine triphosphatase (GTPase) that mediates cytokinesis in bacteria. FtsZ is homologous in structure to eukaryotic tubulin and polymerizes in a similar head-to-tail fashion. The study of tubulin's function in eukaryotic cells has benefited greatly from specific and potent small molecule inhibitors, including colchicine and taxol. Although many small molecule inhibitors of FtsZ have been reported, none has emerged as a generally useful probe for Modulating bacterial cell division. With the goal of establishing a useful and reliable small molecule inhibitor of FtsZ, a broad biochemical cross comparison of reported FtsZ, inhibitors was undertaken. Several of these molecules, including phenolic natural products, are unselective inhibitors that seem to;derive their activity from the formation of microscopic colloids or aggregates. Other compounds, including the natural product viriditoxin and the drug development candidate PC190723, exhibit no inhibition of GTPase activity Using protocols in this work or under published conditions. Of the compounds studied, only zantrin Z3 exhibits good levels of inhibition, maintains activity under conditions that disrupt small molecule aggregates, and provides a platform for exploration of structure-activity relationships (SAR). Preliminary SAR studies have identified slight modifications to the two side chains of this structure that modulate the inhibitory activity of zantrin Z3. Collectively, these studies will help focus future investigations toward the establishment of probes for FtsZ that fill the roles of colchicine and taxol in studies of tubulin.

  DOI：

  10.1021/cb300340j

文献信息

• Comparison of Small Molecule Inhibitors of the Bacterial Cell Division Protein FtsZ and Identification of a Reliable Cross-Species Inhibitor
  作者：David E. Anderson、Michelle B. Kim、Jared T. Moore、Terrence E. O’Brien、Nohemy A. Sorto、Charles I. Grove、Laura L. Lackner、James B. Ames、Jared T. Shaw

  DOI：10.1021/cb300340j

  日期：2012.11.16

  ZFtsZ is a guanosine triphosphatase (GTPase) that mediates cytokinesis in bacteria. FtsZ is homologous in structure to eukaryotic tubulin and polymerizes in a similar head-to-tail fashion. The study of tubulin's function in eukaryotic cells has benefited greatly from specific and potent small molecule inhibitors, including colchicine and taxol. Although many small molecule inhibitors of FtsZ have been reported, none has emerged as a generally useful probe for Modulating bacterial cell division. With the goal of establishing a useful and reliable small molecule inhibitor of FtsZ, a broad biochemical cross comparison of reported FtsZ, inhibitors was undertaken. Several of these molecules, including phenolic natural products, are unselective inhibitors that seem to;derive their activity from the formation of microscopic colloids or aggregates. Other compounds, including the natural product viriditoxin and the drug development candidate PC190723, exhibit no inhibition of GTPase activity Using protocols in this work or under published conditions. Of the compounds studied, only zantrin Z3 exhibits good levels of inhibition, maintains activity under conditions that disrupt small molecule aggregates, and provides a platform for exploration of structure-activity relationships (SAR). Preliminary SAR studies have identified slight modifications to the two side chains of this structure that modulate the inhibitory activity of zantrin Z3. Collectively, these studies will help focus future investigations toward the establishment of probes for FtsZ that fill the roles of colchicine and taxol in studies of tubulin.